ID D9UMN4_STRS3 Unreviewed; 364 AA.
AC D9UMN4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=cholesterol 7-desaturase {ECO:0000256|ARBA:ARBA00026095};
DE EC=1.14.19.21 {ECO:0000256|ARBA:ARBA00026095};
GN ORFNames=SSLG_03994 {ECO:0000313|EMBL:EFL01936.1};
OS Streptomyces sp. (strain SPB78).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFL01936.1, ECO:0000313|Proteomes:UP000005781};
RN [1] {ECO:0000313|EMBL:EFL01936.1, ECO:0000313|Proteomes:UP000005781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB78 {ECO:0000313|EMBL:EFL01936.1,
RC ECO:0000313|Proteomes:UP000005781};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain SPB78.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O
CC + NAD(+); Xref=Rhea:RHEA:51644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17759,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.19.21;
CC Evidence={ECO:0000256|ARBA:ARBA00029355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51645;
CC Evidence={ECO:0000256|ARBA:ARBA00029355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADPH + O2 = 7-dehydrocholesterol + 2 H2O
CC + NADP(+); Xref=Rhea:RHEA:45024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.19.21; Evidence={ECO:0000256|ARBA:ARBA00029369};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45025;
CC Evidence={ECO:0000256|ARBA:ARBA00029369};
CC -!- PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.
CC -!- PATHWAY: Steroid hormone biosynthesis; dafachronic acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00025712}.
CC -!- SIMILARITY: Belongs to the cholesterol 7-desaturase family.
CC {ECO:0000256|ARBA:ARBA00025729}.
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DR EMBL; GG657742; EFL01936.1; -; Genomic_DNA.
DR AlphaFoldDB; D9UMN4; -.
DR STRING; 591157.SSLG_03994; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_037178_1_1_11; -.
DR Proteomes; UP000005781; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR045605; KshA-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR21266:SF60; CHOLESTEROL 7-DESATURASE; 1.
DR PANTHER; PTHR21266; IRON-SULFUR DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF19298; KshA_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 31..132
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 40329 MW; BC7BE02B41D7F8C6 CRC64;
MSRAYGSPLT EGPTPASAST EAPPLPYPSG WAALAFSEEL PVGKVLTRPL AGEDVVLYRL
RSGELRAIRP YCPHLGAHLG LAKLEGDDLV CPFHAFAFAP DGTCVRTGYD TPPPRSPLSR
RHVLEANGAV FVWHHHEDRE PYWTIPAWHE LGHRPARYAA WEFSGHAQEV IENSVDYGHF
ATLHGWKKAE VLEPLTYDGD TFHLTMRATE SAPLIGDFTV DVDVHGYGLG CLHADMYTPR
MGMRMCTMIL PTAIGPHRMQ FRQRNRVAFS EPARLPAPVA KAVSRTAARV FEGLLFKSNI
EFTAADFPIW DSKKYVQPPK LGQGDGPIGP FRRWAKRFYP PEPASAVVAA RDAEAREGAG
RVMR
//
